SASDAR3

PsrP functional binding region

Data type: SASBDB experimental data Status: Published Curve type: Merged Last updated: 2023-05-25T11:21:52.654103+02:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · PsrP functional binding region

Concentration1.1 – 8.7 mg/mlBuffer / pH20 mM sodium citrate 250 mM NaCl 2.5 % Glycerol / 5.5
Experimental temperature10.0 Facility / beamlineDORIS III, DESY / EMBL X33
Wavelength0.15 nmExposure15.0 s × 8

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Functional binding region (187-385) of the pneumococcal serine-rich repeat protein
View sequence
HHHHHHSGNTIVNGAPAINASLNIAKSETKVYTGEGVDSVYRVPIYYKLKVTNDGSKLTFTYTVTYVNPKTNDLGNISSMRPGYSIYNSGTSTQTMLTLGSDLGKPSGVKNYITDKNGRQVLSYNTSTMTTQGSGYTWGNGAQMNGFFAKKGYGLTSSWTVPITGTDTSFTFTPYAARTDRIGINYFNGGGKVVESSTTSQSLSQ
proteinStreptococcus pneumoniaeA0A0H2URK1187–385monomerMolecule count 122.12 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
12129[3]0.198385–6.02138 1/nmHas uncertainty columnMissing 00sasbdb/entries/r3/sasdar3/source/SASDAR3.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)7.7—nm
i0Guinier16.7——
i0P(r)16.34——
mwExperimental18.0—kDa
mwPorod23.0—kDa
porod_volumePorod37.0—nm³
rgGuinier2.27—nm
rgP(r)2.25—nm

These values are reported by SASBDB; SAXSdb did not recalculate them from the experimental curve.

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3. Source Fits and Models Source Fits & Models

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4. Source File Index Source Files

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5. Experiment Description and Publication Experiment & Publication

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6. Complete Source Record Complete Source Record

The following content comes directly from the SASBDB entry. Missing values are shown as “—”; SAXSdb does not infer undeclared units.

Open the original SASBDB entry

Buffer and Sample Properties

Buffer name20 mM sodium citrate 250 mM NaCl 2.5 % GlycerolBuffer concentration20.0 mM
pH5.5AdditivesNaCl 250.000 mM, glycerol 2.500 %
Buffer descriptionbuffer for BR(187-385)
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2011-07-02Storage / measurement temperature10.0 / 10.0
Exposure time15.0Frames8
Wavelength0.15Sample-to-detector distance2.7
SourceX-ray synchrotronDetectorPilatus 1M-W
Facility / beamlineDORIS III, DESY / EMBL X33 · Hamburg, Germany
q range0.198 – 6.021Sample volume / flow rate— / —

Original SASBDB Plots

Experimental I(q)
Experimental I(q)
Experimental I(q), log-log
Experimental I(q), log-log
Guinier plot
Guinier plot
Kratky plot
Kratky plot
P(r) plot
P(r) plot

Downloadable Files

CategoryFileStatusSizeChecksumDownload and View
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full_entry_zipsasbdb/entries/r3/sasdar3/source/SASDAR3.zipdownloaded201465edc21b9a83b4abe32e0c5fd8dc4f6e99e9f854905e67f4d32f27301e44282f7cDownloadView source fileSource site
pddfsasbdb/entries/r3/sasdar3/source/SASDAR3.outdownloaded35596ebe1923deca3841c6e02a70a01291aa84ff7efa3afb269c3530497bca93be5ecDownloadView source fileSource site
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full_entry_zip:source record and ZIP contents (9 items)
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All source fields (unfiltered)

Every source field is expanded here, including empty values, list members and fields already shown above.

summary.json:208 field values
Field pathRaw value
codeSASDAR3
statusPublished
type_of_curveMerged
angular_unit1/nm
project.titleThe basic keratin 10-binding domain of the virulence-associated pneumococcal serine-rich protein PsrP adopts a novel MSCRAMM fold.
project.publication.titleThe basic keratin 10-binding domain of the virulence-associated pneumococcal serine-rich protein PsrP adopts a novel MSCRAMM fold.
project.publication.author_listSchulte T, Löfling J, Mikaelsson C, Kikhney A, Hentrich K, Diamante A, Ebel C, Normark S, Svergun D, Henriques-Normark B, Achour A
project.publication.journalOpen Biol
project.publication.doi10.1098/rsob.130090
project.publication.pmid24430336
project.publication.published_date2014 Jan 15
project.statusreleased
project.submitted_datenull
project.released_date2014-07-31
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDAR3.out
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDAR3.dat
intensities_log_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDAR3_dat_img.png
intensities_kratky_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDAR3_kratky_img.png
pddf_plothttps://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDAR3_pofr_img.png
intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDAR3_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDAR3.sascif
experiment.instrument.detector.typeCustom-built
experiment.instrument.detector.namePilatus 1M-W
experiment.instrument.detector.resolution0.172
experiment.instrument.nameDORIS III, DESY
experiment.instrument.cityHamburg
experiment.instrument.countryGermany
experiment.instrument.beamline_nameEMBL X33
experiment.instrument.beam_geometry0.60
experiment.instrument.type_of_sourceX-ray synchrotron
experiment.instrument.point_sourcenull
experiment.instrument.line_collimationnull
experiment.instrument.sample_path_lengthnull
experiment.instrument.line_collimation_slitlengthnull
experiment.instrument.line_collimation_integrationwidthnull
experiment.instrument.xray_energynull
experiment.instrument.beam_profile_ahnull
experiment.instrument.beam_profile_alnull
experiment.sample.molecule[0].long_nameFunctional binding region (187-385) of the pneumococcal serine-rich repeat protein
experiment.sample.molecule[0].short_namePsrP BR(187-385)
experiment.sample.molecule[0].sequenceHHHHHHSGNTIVNGAPAINASLNIAKSETKVYTGEGVDSVYRVPIYYKLKVTNDGSKLTFTYTVTYVNPKTNDLGNISSM RPGYSIYNSGTSTQTMLTLGSDLGKPSGVKNYITDKNGRQVLSYNTSTMTTQGSGYTWGNGAQMNGFFAKKGYGLTSSWTVPITGTDTSFTFTPYAARTDRIGINYFNGGGKVVESSTTSQSLSQ
experiment.sample.molecule[0].organismStreptococcus pneumoniae
experiment.sample.molecule[0].uniprot_codeA0A0H2URK1
experiment.sample.molecule[0].uniprot_range_first187
experiment.sample.molecule[0].uniprot_range_last385
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMTETVEDKVSHSITGLDILKGIVAAGAVISGTVATQTKVFTNESAVLEKTVEKTDALATN DTVVLGTISTSNSASSTSLSASESASTSASESASTSASTSASTSASESASTSASTSISAS STVVGSQTAAATEATAKKVEEDRKKPASDYVASVTNVNLQSYAKRRKRSVDSIEQLLASI KNAAVFSGNTIVNGAPAINASLNIAKSETKVYTGEGVDSVYRVPIYYKLKVTNDGSKLTF TYTVTYVNPKTNDLGNISSMRPGYSIYNSGTSTQTMLTLGSDLGKPSGVKNYITDKNGRQ VLSYNTSTMTTQGSGYTWGNGAQMNGFFAKKGYGLTSSWTVPITGTDTSFTFTPYAARTD RIGINYFNGGGKVVESSTTSQSLSQSKSLSVSASQSASASASTSASASASTSASASASTS ASASASTSASVSASTSASASASTSASASASTSASESASTSASASASTSASASASTSASAS ASTSASESASTSASASASTSASESASTSASASASTSASASASTSASGSASTSTSASASTS ASASASTSASASASISASESASTSASESASTSTSASASTSASESASTSASASASTSASAS ASTSASASASTSASASTSASESASTSASASASTSASASASTSASASASTSASASASTSAS VSASTSASASASTSASASASTSASESASTSASASASTSASASASTSASASASTSASASAS TSASASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASASISAS ESASTSASASASTSASASASTSASASASTSASESASTSASASASTSASASASTSASASAS TSASASASTSASASASTSASASASTSASESASTSASASASTSASESASTSASASASTSAS ASASTSASASASTSASASASTSASASASTSASASASTSASASTSASESASTSASASASTS ASASASTSASASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASAS ASISASESASTSASASASTSASVSASTSASASASTSASESASTSASASASTSASESASTS ASASASTSASASASISASESASTSASASASTSASASASTSASASASTSASESASTSTSAS ASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASTSASESASTSAS ASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASAS TSASESASTSASASASTSASASASTSASASASTSASASASTSASVSASTSASESASTSAS ASASTSASASASTSASESASTSASASASTSASESASTSASASASTSASASASTSASASAS TSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSAS ASASTSASASASTSASASASISASESASTSASASASTSASASASTSASVSASTSASASAS TSASASASISASESASTSASASASTSASASASTSASASASTSASASASISASESASTSAS ASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASAS TSASASASTSASESASTSASASASTSASASASTSASASASTSASVSASTSASESASTSAS ASASTSASASASTSASASASTSASESASTSASASASTSASASASTSASESASTSASASAS TSASASASTSASASASTSASASASASTSASASASTSASASASTSASASASISASESASTS ASESASTSTSASASTSASESASTSASASASTSASASASTSASASASTSASASTSASESAS TSASASASTSASASASTSASASASTSASASASTSASASASTSASVSASTSASASASTSAS ASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASASTSASESAS TSASASASTSASASASTSASASASTSASASASTSASASASISASESASTSASASASTSAS ASASTSASASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASAS TSASASASTSASESASTSASASASTSASESASTSASASASTSASASASTSASASASTSAS ASASTSASASASTSASASASTSASASTSASESASTSASASASTSASASASTSASASASTS ASESASTSASASASTSASASASTSASASASTSASASASTSASASASISASESASTSASAS ASTSASVSASTSASASASTSASESASTSASASASTSASESASTSASASASTSASASASIS ASESASTSASASASTSASASASTSASASASTSASESASTSTSASASTSASESASTSASAS ASTSASASASTSASASASTSASASASTSASASTSASESASTSASASASTSASASASTSAS ASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASAS TSASASASTSASESASTSASASASTSASASASTSASASASTSASVSASTSASESASTSAS ASASTSASASASTSASASASTSASESASTSASASASTSASASASTSASESASTSASASAS TSASASASTSASASASTSASASASASTSASASASTSASASASTSASASASISASESASTS ASASASASTSASASASTSASASASTSASASASISASESASTSASESASTSTSASASTSAS ESASTSASASASTSASASASTSASASASTSASASTSASESASTSASASASTSASASASTS ASASASTSASASASTSASASASTSASVSASTSASASASTSASASASTSASESASTSASAS TSASESASTSASASASTSASASASTSASASASTSASESASTSASASASTSASASASTSAS ESASTSASASASTSASASASTSASASASTSASESASTSASASASTSASESASTSASASAS TSASASASTSASGSASTSTSASASTSASASASTSASASASISASESASTSASESASTSTS ASASTSASESASTSASASASTSASASASTSASASASTSASASTSASESASTSASASASTS ASASASTSASASASTSASASASTSASVSASTSASASASTSASASASTSASESASTSASAS ASTSASASASTSASASASTSASASASTSASASASTSASESASTSASASASTSASASASTS ASASASTSASASASTSASASASISASESASTSASASASTSASASASTSASASASTSASES ASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASESASTS ASASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASASTSASAS ASTSASASTSASESASTSASASASTSASASASTSASASASTSASESASTSASASASTSAS ASASTSASASASTSASASASTSASASASISASESASTSASASASTSASVSASTSASASAS TSASESASTSASASASTSASESASTSASASASTSASASASISASESASTSASASASTSAS ASASTSASASASTSASESASTSTSASASTSASESASTSASASASTSASASASTSASASAS TSASASASTSASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASAS ASTSASASASTSASASASTSASASASTSASESASTSASASASTSASASASTSASASASTS ASASASTSASVSASTSASESASTSASASASTSASASASTSASESASTSASASASTSASES ASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTS ASASASTSASASASTSASASASTSASASASTSASASASTSASASASISASESASTSASAS ASTSASASASTSASVSASTSASASASTSASASASISASESASTSASASASTSASASASTS ASASASTSASASASISASESASTSASASASTSASASASTSASASASTSASASASTSASAS ASTSASASASTSASASASTSASASASTSASASASTSASESASTSASASASTSASASASIS ASESASTSASASASTSASASASTSASASASTSASESASTSTSASASTSASESASTSASAS ASTSASASASTSASASASTSASASASTSASASTSASESASTSASASASTSASASASTSAS ASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASESASTSASASAS TSASASASTSASASASTSASASASTSASVSASTSASESASTSASASASTSASASASTSAS ESASTSASASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASAS TSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSAS ASASISASESASTSASASASTSASASASTSASVSASTSASASASTSASASASISASESAS TSASASASTSASASASTSASASASTSASASASISASESASTSASASASTSASASASTSAS ASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASAS TSASASASTSASASASTSASASASTSASASASTSVSNSANHSNSQVGNTSGSTGKSQKEL PNTGTESSIGSVLLGVLAAVTGIGLVAKRRKRDEEE
experiment.sample.molecule[0].mw22.12
experiment.sample.molecule[0].total_mw22.12
experiment.sample.molecule[0].number_molecules1
experiment.sample.molecule[0].complex_statenull
experiment.sample.molecule[0].deuterationnull
experiment.sample.molecule[0].molecule_sourcebiological
experiment.sample.molecule[0].molecule_descriptionnull
experiment.sample.buffer.name20 mM sodium citrate 250 mM NaCl 2.5 % Glycerol
experiment.sample.buffer.concentration_unitmM
experiment.sample.buffer.commentbuffer for BR(187-385)
experiment.sample.buffer.additiveNaCl 250.000 mM, glycerol 2.500 %
experiment.sample.buffer.concentration20.0
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph5.5
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.namePsrP functional binding region
experiment.sample.ext_coefficientnull
experiment.sample.contrastnull
experiment.sample.specific_volnull
experiment.sample.dry_volnull
experiment.sample.absorbptionnull
experiment.sample.deuterationnull
experiment.sample.mixturenull
experiment.contributor[0].affiliation[0].short_nameEMBL-Hamburg
experiment.contributor[0].affiliation[0].addressNotkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany
experiment.contributor[0].affiliation[0].full_nameEuropean Molecular Biology Laboratory (EMBL) - Hamburg outstation
experiment.contributor[0].affiliation[0].webpagehttp://www.embl-hamburg.de/index.php
experiment.contributor[0].contributor_nameAl
experiment.contributor[0].contributor_surnameKikhney
experiment.contributor[0].orcidhttps://orcid.org/0000-0003-1321-3956
experiment.concentration_methodnull
experiment.concentration_unitmg/ml
experiment.date2011-07-02
experiment.storage_temperature10.0
experiment.cell_temperature10.0
experiment.exposure_time15.0
experiment.number_of_frames8
experiment.wavelength0.15
experiment.sample_detector_distance2.7
experiment.concentration_min1.1
experiment.concentration_max8.7
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.198
experiment.s_max6.021
experiment.total_exposure_timenull
experiment.seccolumnnull
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View the complete summary.json source
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    "title": "The basic keratin 10-binding domain of the virulence-associated pneumococcal serine-rich protein PsrP adopts a novel MSCRAMM fold.",
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      "title": "The basic keratin 10-binding domain of the virulence-associated pneumococcal serine-rich protein PsrP adopts a novel MSCRAMM fold.",
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